ID   CBPYA_LEPMJ             Reviewed;         543 AA.
AC   E5A7I6;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=CPYA; ORFNames=Lema_P088200;
OS   Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS   (Blackleg fungus) (Phoma lingam).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC   Leptosphaeria; Leptosphaeria maculans species complex.
OX   NCBI_TaxID=985895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8;
RX   PubMed=21326234; DOI=10.1038/ncomms1189;
RA   Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA   Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA   Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA   Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA   Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA   Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA   Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA   Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT   "Effector diversification within compartments of the Leptosphaeria maculans
RT   genome affected by Repeat-Induced Point mutations.";
RL   Nat. Commun. 2:202-202(2011).
CC   -!- FUNCTION: Vacuolar carboxypeptidase involved in degradation of small
CC       peptides. Digests preferentially peptides containing an aliphatic or
CC       hydrophobic residue in P1' position, as well as methionine, leucine or
CC       phenylalanine in P1 position of ester substrate (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of a C-terminal amino acid with broad specificity.;
CC         EC=3.4.16.5; Evidence={ECO:0000255|PROSITE-ProRule:PRU10074};
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; FP929136; CBX99581.1; -; Genomic_DNA.
DR   RefSeq; XP_003843060.1; XM_003843012.1.
DR   AlphaFoldDB; E5A7I6; -.
DR   SMR; E5A7I6; -.
DR   STRING; 985895.E5A7I6; -.
DR   MEROPS; S10.001; -.
DR   PRIDE; E5A7I6; -.
DR   EnsemblFungi; CBX99581; CBX99581; LEMA_P088200.1.
DR   GeneID; 13289211; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   InParanoid; E5A7I6; -.
DR   OMA; GDWMKPF; -.
DR   OrthoDB; 625787at2759; -.
DR   Proteomes; UP000002668; Genome.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR008442; Propeptide_carboxypepY.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802; PTHR11802; 1.
DR   Pfam; PF05388; Carbpep_Y_N; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Signal; Vacuole; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..128
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407451"
FT   CHAIN           129..543
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407452"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        460
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        519
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        213
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        508
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        182..421
FT                   /evidence="ECO:0000250"
FT   DISULFID        316..330
FT                   /evidence="ECO:0000250"
FT   DISULFID        340..363
FT                   /evidence="ECO:0000250"
FT   DISULFID        347..356
FT                   /evidence="ECO:0000250"
FT   DISULFID        385..391
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   543 AA;  61006 MW;  9D60B7CBE773A600 CRC64;
     MKVATSALLV GAVSASVGPQ QQVLKFPDSF SELKEGAWSK PLHKLEESLK TLTGEARAVW
     DEVAMMFPES FEKAAFFSEP KPHTRKHDSE WDHIIKGADI QNVWVENKNG DKEREIDGKL
     ENYSMRTKKV DPSVLGVDKV KQYSGYLDDE EEDKHLFYWF FESRNDPKND PVVLWLNGGP
     GCSSLTGLFM ELGPASITKD GKIKHNPYSW NSNASVIFLD QPVNVGYSYS SGQVSNTVAA
     GKDIYALLTL FFKQFPEYAE QSFHISGESY AGHYIPVFAS EILSHKKRNI NLQSVLIGNG
     LTDGLTQYEY YRPMACGEGG WPAVLDESQC KAMDNAYPRC ASLIENCYNS ESVWSCVPAS
     IYCNNAMIGP YQRTGQNVYD IRKPCGSNSL CYDELDWIQA YLNKKEVMKA VGAEISSYES
     CNFDINRNFL LQGDWMKPFH RIVPGLLAEI PVLIYAGDAD YICNWLGNKA WTEALEWPGQ
     KDYNKAEMED FKIDGKGEAV GQVKSSGNFT FLKIHAGGHM VPYDQPEASL TMLNRWLAGD
     FWA